ID A0A1A8T0P1_9GAMM Unreviewed; 867 AA.
AC A0A1A8T0P1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:SBS24683.1};
GN ORFNames=MAQ5080_00074 {ECO:0000313|EMBL:SBS24683.1};
OS Marinomonas aquimarina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=295068 {ECO:0000313|EMBL:SBS24683.1, ECO:0000313|Proteomes:UP000092627};
RN [1] {ECO:0000313|EMBL:SBS24683.1, ECO:0000313|Proteomes:UP000092627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5080 {ECO:0000313|EMBL:SBS24683.1,
RC ECO:0000313|Proteomes:UP000092627};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FLOC01000001; SBS24683.1; -; Genomic_DNA.
DR RefSeq; WP_067203937.1; NZ_LTAV01000001.1.
DR AlphaFoldDB; A0A1A8T0P1; -.
DR STRING; 295068.MAQ5080_00074; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000092627; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000092627};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 96638 MW; CFC0F49B70BB7A47 CRC64;
MRIDRLTSKL QIALSDAQSV ALGQDHNYIE AVHVLMALLD QQGGGVRPIL QQAGVQMAKF
REELGSILDR MPKVTNHDGN VQMSPELGRL LNLADKEAQK RKDQYISSEL LLLAMFDGKD
DVAKALKATG VTKADIAAVI DSVRGGETVN DPNAEESRQS LDKFTVDLTA RAAEGRLDPV
IGRDDEIRRT IQVLQRRRKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKNKRVLSL
DMGALIAGAK YRGEFEERLK SVLNELAKQE GQIILFIDEI HTMVGAGKSE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVEE PSVLDSIAIL RGLKERYEVH
HGVDITDSAI IAAAKLSQRY ITDRQLPDKA IDLIDEAASR IRMEMDSKPE EMDRLERRLI
QLKIEQEALK KEKDKASKQR LTELEDDIEA LEKQFSDLEE IWNAEKAALQ GAQKLKEELE
GVRHEMEEAR RQGNLAKMSE LQYGVIPMLE AEIEKAAQAE ESEAQTQLLK NRVTEEEIAT
VVSRWTGIPV DKMLEGERDK LLRMEDALHE SVIGQDEAVT AVSNAVRRSR SGLADPNRPN
GSFLFLGPTG VGKTELCKSL AKFLFDTEQA MVRVDMSEFM EKHSVARLIG APPGYVGYEE
GGYLTEAVRR RPYSVLLLDE VEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FRNTVVVMTS
NLGSDMIQEY RSNDEYEAIK NKVMEVVGTH FRPEFINRID ETVVFHPLMQ SQIKGIAKIQ
LAHLNDRLTE MGMSINLSEA AMERLAEVGY DPVYGARPLK RAIQQWIENP LANELLGGKF
VAGDLIQVDV NEQGMTFAAL PEAQQAS
//